Target Name: CAMKK1
NCBI ID: G84254
Review Report on CAMKK1 Target / Biomarker Content of Review Report on CAMKK1 Target / Biomarker
CAMKK1
Other Name(s): calcium/calmodulin dependent protein kinase kinase 1 | CaM-KK alpha | CaMKK alpha | CaM-KK 1 | CAMKKA | caM-KK 1 | Calcium/calmodulin dependent protein kinase kinase 1, transcript variant 1 | Calcium/calmodulin-dependent protein kinase kinase 1 (isoform a) | Calcium/calmodulin-dependent protein kinase kinase alpha | calcium/calmodulin-dependent protein kinase kinase alpha | CaM-kinase kinase 1 | caM-KK alpha | CAMKK alpha protein | CaM-kinase IV kinase | caMKK 1 | CaMKK 1 | KKCC1_HUMAN | CaM-kinase kinase alpha | caM-kinase IV kinase | CAMKK1 variant 1 | Calcium/calmodulin-dependent protein kinase kinase 1 | caM-kinase kinase alpha | caM-kinase kinase 1 | calcium/calmodulin-dependent protein kinase kinase 1, alpha

CAMKK1: A Calcium-Dependent Protein Kinase for Therapeutic Targeting

Introduction

CAMKK1 (calcium/calmodulin dependent protein kinase 1) is a protein that plays a crucial role in cellular signaling pathways, particularly in the regulation of calcium homeostasis. CAMKK1 is a serine protein that is expressed in various tissues, including brain, muscle, and pancreas , and functions as a protein kinase, activating other proteins in the cell. Its function is highly dependent on calcium ions, which are essential for various cellular processes. However, aberrant levels of calcium ions have been implicated in various diseases, including Alzheimer's disease, Parkinson's disease, and diabetes. Therefore, targeting CAMKK1 could be a promising strategy for the development of new therapeutic approaches for these diseases.

CAMKK1 Structure and Function

CAMKK1 is a 21-kDa protein that consists of 215 amino acid residues. It has a unique catalytic mechanism, as it uses both calcium ions and calmodulin to generate a high-energy transition that activates the protein. The protein has a three-dimensional structure that is composed of a catalytic domain and a regulatory domain. The catalytic domain is responsible for the protein's catalytic activity, while the regulatory domain plays a role in regulating the activity of the protein.

The catalytic domain of CAMKK1 is characterized by a conserved catalytic core that is known as the \"alpha-helices\" region. This region has a characteristic Rossmann-fold that allows the protein to bind to calcium ions and calmodulin. The catalytic core is responsible for the protein's catalytic activity, as it provides a platform for the formation of a high-energy transition that activates the protein.

The regulatory domain of CAMKK1 is characterized by a unique N-terminal region that is known as the \"zinc finger\" domain. This domain has been implicated in the regulation of various cellular processes, including cell signaling pathways and protein function. The zinc Finger domain is responsible for the regulation of the protein's activity, as it interacts with various cellular components to regulate its function.

CAMKK1 is regulated by various factors, including calcium ions, calmodulin, and various signaling pathways. Its activity is highly dependent on the levels of these factors, which are essential for the regulation of cellular processes. For example, increased levels of calcium ions or calmodulin have been shown to activate the activity of CAMKK1, while decreased levels of these factors have an inhibitory effect on the protein's activity.

CAMKK1 has been implicated in various diseases, including Alzheimer's disease, Parkinson's disease, and diabetes. Aberrant levels of calcium ions have been shown to contribute to the development and progression of these diseases. For example, increased levels of calcium ions have been shown to contribute to the development of Alzheimer's disease, as they can cause the buildup of beta-amyloid plaques and neurofibrillary tangles in the brain. Similarly, decreased levels of calcium ions have been shown to contribute to the development and progression of Parkinson's disease, as they can cause the loss of dopamine-producing neurons in the brain.

Targeting CAMKK1

The targeting of CAMKK1 as a drug target or biomarker has the potential to treat various diseases. One approach to targeting CAMKK1 is to develop small molecules that can inhibit the protein's activity. Such compounds have been shown to be effective in various cellular assays, including cell signaling pathways and protein function.

Another approach to targeting CAMKK1 is to develop antibodies that can specifically bind to the protein. Such antibodies have been shown to be effective in various cellular assays, including

Protein Name: Calcium/calmodulin Dependent Protein Kinase Kinase 1

Functions: Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death

The "CAMKK1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about CAMKK1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets

CAMKK2 | CAMKMT | CAMKV | CAMLG | CAMP | cAMP Phosphodiesterase | cAMP Responsive Element Binding Protein (CREB) | cAMP-Dependent protein kinase (PKA) | CAMSAP1 | CAMSAP2 | CAMSAP3 | CAMTA1 | CAMTA2 | CAND1 | CAND1.11 | CAND2 | Cannabinoid receptor | CANT1 | CANX | Cap-binding complex | CAP1 | CAP2 | CAPG | CAPN1 | CAPN10 | CAPN10-DT | CAPN11 | CAPN12 | CAPN13 | CAPN14 | CAPN15 | CAPN2 | CAPN3 | CAPN5 | CAPN6 | CAPN7 | CAPN8 | CAPN9 | CAPNS1 | CAPNS2 | CAPRIN1 | CAPRIN2 | CAPS | CAPS2 | CAPSL | CAPZA1 | CAPZA2 | CAPZA3 | CAPZB | Carbonic Anhydrase | Carbonic Anhydrase V | Carboxylesterase | Carboxypeptidase A | Carboxypeptidase B | Carboxypeptidase N | Carcinoembryonic Antigen-Related Cell Adhesion Molecule (CEA) | CARD10 | CARD11 | CARD14 | CARD16 | CARD17P | CARD18 | CARD19 | CARD6 | CARD8 | CARD8-AS1 | CARD9 | Cardiac Troponin | CARF | CARHSP1 | CARM1 | CARMAL | CARMIL1 | CARMIL2 | CARMIL3 | CARMN | Carnitine O-Palmitoyltransferase (CPT) | Carnitine O-Palmitoyltransferase 1 (CPT-1) | Carnitine O-palmitoyltransferase 2 | CARNMT1 | CARNS1 | CARS1 | CARS1-AS1 | CARS2 | CARTPT | CASC11 | CASC15 | CASC16 | CASC17 | CASC18 | CASC19 | CASC2 | CASC20 | CASC21 | CASC22 | CASC3 | CASC6 | CASC8 | CASC9 | CASD1